Abstract
We present a molecular-scale simulation study of the structural transitions between helicoidal, helical, and tubular geometries in supramolecular beta-sheet tapes. Such geometries have been observed in different self-assembled amyloid systems (based on either natural or synthetic peptides) for which the beta-sheet tapes represent the simplest fibrillar aggregates. A coarse-grained model for the beta-sheet tapes is proposed, with chiral degrees of freedom and asymmetrical chemical properties, which provides a quantitative characterization of the structural transitions. A quantitative connection is established between the molecular properties and the elastic parameters of the supramolecular tapes. (c) 2008 American Institute of Physics.
| Original language | English |
|---|---|
| Article number | 195105 |
| Pages (from-to) | - |
| Number of pages | 7 |
| Journal | Journal of Chemical Physics |
| Volume | 128 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 12 May 2008 |
Keywords
- amphiphilic assemblies
- molecular dynamics
- helical ribbons
- peptide
- origin
- proteins
- forces